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Science 12 January 2001:
Vol. 291. no. 5502, pp. 316 - 319
DOI: 10.1126/science.291.5502.316
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Reports

Role of ER Export Signals in Controlling Surface Potassium Channel Numbers

Dzwokai Ma,1 Noa Zerangue,1 Yu-Fung Lin,1 Anthony Collins,2 Mei Yu,1 Yuh Nung Jan,1 Lily Yeh Jan1*

Little is known about the identity of endoplasmic reticulum (ER) export signals and how they are used to regulate the number of proteins on the cell surface. Here, we describe two ER export signals that profoundly altered the steady-state distribution of potassium channels and were required for channel localization to the plasma membrane. When transferred to other potassium channels or a G protein-coupled receptor, these ER export signals increased the number of functional proteins on the cell surface. Thus, ER export of membrane proteins is not necessarily limited by folding or assembly, but may be under the control of specific export signals.

1 Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94143-0725, USA.
2 College of Pharmacy, Oregon State University, Corvallis, OR 97331-3507, USA
*   To whom correspondence should be addressed. E-mail: gkw{at}itsa.ucsf.edu

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L. Iodice, S. Sarnataro, and S. Bonatti (2001)
J. Biol. Chem. 276, 28920-28926
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Calmodulin Regulates Assembly and Trafficking of SK4/IK1 Ca2+-activated K+ Channels.
W. J. Joiner, R. Khanna, L. C. Schlichter, and L. K. Kaczmarek (2001)
J. Biol. Chem. 276, 37980-37985
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Science. ISSN 0036-8075 (print), 1095-9203 (online)